1YHW
Crystal Structure of PAK1 kinase domain with one point mutations (K299R)
Summary for 1YHW
| Entry DOI | 10.2210/pdb1yhw/pdb |
| Related | 1YHV |
| Descriptor | Serine/threonine-protein kinase PAK 1 (2 entities in total) |
| Functional Keywords | kinase; active conformation; activation loop; atp binding site, signaling protein, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q13153 |
| Total number of polymer chains | 1 |
| Total formula weight | 33273.23 |
| Authors | Lei, M.,Robinson, M.A.,Harrison, S.C. (deposition date: 2005-01-10, release date: 2005-05-24, Last modification date: 2024-02-14) |
| Primary citation | Lei, M.,Robinson, M.A.,Harrison, S.C. The Active Conformation of the PAK1 Kinase Domain Structure, 13:769-778, 2005 Cited by PubMed Abstract: The p21-activated kinases (PAKs) participate in cytoskeletal control networks, downstream of Rho-family GTPases. A structure of PAK1 in an autoregulated, "off" state showed that a regulatory region, N-terminal to the kinase domain, forces the latter into an inactive conformation, prevents phosphorylation of Thr423 in the activation loop, and promotes dimerization. We have now determined structures at 1.8 A resolution for the free PAK1 kinase domain, with a mutation in the active site that blocks enzymatic activity, and for the same domain with a "phosphomimetic" mutation in the activation loop. The two very similar structures show that even in the absence of a phosphorylated Thr423, the kinase has an essentially active conformation. When Cdc42 binds the regulatory region and dissociates the dimer, PAK1 will be in an "intermediate-active" state, with a capacity to phosphorylate itself or other substrates even prior to modification of its activation loop. PubMed: 15893667DOI: 10.1016/j.str.2005.03.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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